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Database: UniProt
Entry: Q38AE1_TRYB2
LinkDB: Q38AE1_TRYB2
Original site: Q38AE1_TRYB2 
ID   Q38AE1_TRYB2            Unreviewed;       497 AA.
AC   Q38AE1;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   SubName: Full=Protein disulfide isomerase {ECO:0000313|EMBL:EAN78229.1};
DE            EC=5.3.4.1 {ECO:0000313|EMBL:EAN78229.1};
GN   ORFNames=Tb10.6k15.2290 {ECO:0000313|EMBL:EAN78229.1};
OS   Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=185431 {ECO:0000313|EMBL:EAN78229.1, ECO:0000313|Proteomes:UP000008524};
RN   [1] {ECO:0000313|EMBL:EAN78229.1, ECO:0000313|Proteomes:UP000008524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:EAN78229.1,
RC   ECO:0000313|Proteomes:UP000008524};
RX   PubMed=16020726; DOI=10.1126/science.1112642;
RA   Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA   Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA   Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA   Alsmark U.C., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA   Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA   Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA   Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA   Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA   Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA   Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA   Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA   Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA   Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA   Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA   Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA   Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA   Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA   Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.;
RT   "The genome of the African trypanosome Trypanosoma brucei.";
RL   Science 309:416-422(2005).
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|RuleBase:RU004208}.
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DR   EMBL; CM000208; EAN78229.1; -; Genomic_DNA.
DR   RefSeq; XP_823057.1; XM_817964.1.
DR   AlphaFoldDB; Q38AE1; -.
DR   SMR; Q38AE1; -.
DR   STRING; 185431.Q38AE1; -.
DR   PaxDb; 5691-EAN78229; -.
DR   GeneID; 3663041; -.
DR   KEGG; tbr:Tb10.6k15.2290; -.
DR   VEuPathDB; TriTrypDB:Tb927.10.8230; -.
DR   eggNOG; KOG0190; Eukaryota.
DR   InParanoid; Q38AE1; -.
DR   OMA; FRSKHEP; -.
DR   OrthoDB; 5399045at2759; -.
DR   Proteomes; UP000008524; Chromosome 10.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
DR   CDD; cd02961; PDI_a_family; 1.
DR   CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR   CDD; cd02982; PDI_b'_family; 1.
DR   CDD; cd02981; PDI_b_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR   InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR01126; pdi_dom; 1.
DR   PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR   PANTHER; PTHR18929:SF246; PROTEIN DISULFIDE-ISOMERASE; 1.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 4.
DR   PROSITE; PS00194; THIOREDOXIN_1; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:EAN78229.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008524};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..497
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004221835"
FT   DOMAIN          8..124
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          334..455
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          461..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   497 AA;  55580 MW;  3BEAA2AF9FA6C76D CRC64;
     MRAIFLVALA LATMRESTAE SLKLTKENFN ETIAKSEIFL VKFYVDTCGY CQMLAPEWEK
     AANETIDNAL MGEVDCHSQP ELAANFSIRG YPTIILFRNG KEAEHYGGAR TKDDIIKYIK
     ANVGPAVTPA SNAEEVTRAK EEHDVVCVGL TASNSTSLST TLAEAAQSFR VSLKFFEAEP
     KLFPDEKPET IVVYRKGGEK EVYDGPMEVE KLTEFLQISR VAFGGEITPE NYQYYSVIKR
     PVGWAMVKPN ETASIELKES LTEVGKKMRS HMVVLWVNIS KHPVWRDFGV PEDAKYPAFL
     AIHWGANYLH STAEVVTRES LEKFILEFAA GRVEPTIKSL PVPEVETVDG KTTIVAKTMQ
     KHLTSGKDML ILFFAPWCGH CKNFAPTFDK IAKEFDATDL IVAELDATAN YVNSSTFTVT
     AFPTVFFVPN GGKPVVFEGE RSFENVYEFV RKHVTTFKVS EKPANVTEEK KSEEENKSSR
     SNESNDSNES NVDKQDL
//
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